ID A6U7C8_SINMW Unreviewed; 172 AA.
AC A6U7C8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN OrderedLocusNames=Smed_0702 {ECO:0000313|EMBL:ABR59558.1};
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR59558.1, ECO:0000313|Proteomes:UP000001108};
RN [1] {ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR59558.1, ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|EMBL:ABR59558.1,
RC ECO:0000313|Proteomes:UP000001108};
RX PubMed=21304680; DOI=10.4056/sigs.43526;
RA Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT "Complete genome sequence of the Medicago microsymbiont Ensifer
RT (Sinorhizobium) medicae strain WSM419.";
RL Stand. Genomic Sci. 2:77-86(2010).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU000393};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR EMBL; CP000738; ABR59558.1; -; Genomic_DNA.
DR RefSeq; WP_011974904.1; NC_009636.1.
DR RefSeq; YP_001326393.1; NC_009636.1.
DR AlphaFoldDB; A6U7C8; -.
DR STRING; 366394.Smed_0702; -.
DR GeneID; 61609978; -.
DR KEGG; smd:Smed_0702; -.
DR PATRIC; fig|366394.8.peg.3806; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_8_1_5; -.
DR OrthoDB; 5431326at2; -.
DR Proteomes; UP000001108; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..172
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002702615"
FT DOMAIN 40..171
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 172 AA; 17915 MW; E36612B03B0D4ED9 CRC64;
MMRTMIAIAV AAGMASAASA QQSSQTATAE FMGKDGTDIG RATLTAGGKG VLIEMEISGL
PKDSWVAFHA HEMGRCDPKE GFESAGKHFA GKDENTEHGF LAANGPHAGD MPNQYVGADG
TLRAHVFNSF VSLDDAGNGL RGRALVIHMH SDDNRSQPSG DAGDRLACAV VK
//
